PT  - JOURNAL ARTICLE
AU  - Ian R. Monk
AU  - Torsten Seemann
AU  - Benjamin P. Howden
AU  - Timothy P. Stinear
TI  - Refutation: <em>Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus</em>
AID  - 10.1101/058842
DP  - 2016 Jan 01
TA  - bioRxiv
PG  - 058842
4099  - http://biorxiv.org/content/early/2016/06/14/058842.short
4100  - http://biorxiv.org/content/early/2016/06/14/058842.full
AB  - In a recent report in Nature Communications, Ji et al., (2016)1 describe the structure of the extracytoplasmic Per-Arnt-Sim (PAS) domain of WalK (WalKEC-PAS), the sensor kinase of the essential two-component regulator WalKR in Staphylococcus aureus1. The authors make two independent walK S. aureus mutants by changing two amino acid residues they postulate from structural analysis and comparisons might be important for signal transduction. We have also been exploring the function of WalKR and were surprised by the striking phenotypic impact of these single amino acid substitutions in the WalK sensor, which are contrary to our own (unpublished) observations.